P3C2G_HUMAN
ID P3C2G_HUMAN Reviewed; 1445 AA.
AC O75747; A1L3U0;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Phosphatidylinositol 3-kinase C2 domain-containing subunit gamma {ECO:0000305};
DE Short=PI3K-C2-gamma;
DE Short=PtdIns-3-kinase C2 subunit gamma;
DE EC=2.7.1.137 {ECO:0000250|UniProtKB:O70173};
DE EC=2.7.1.154 {ECO:0000250|UniProtKB:O70173};
DE AltName: Full=Phosphoinositide 3-kinase-C2-gamma;
GN Name=PIK3C2G;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT LEU-911.
RC TISSUE=Liver, Mammary gland, and Prostate;
RX PubMed=9878262; DOI=10.1006/geno.1998.5621;
RA Rozycka M., Lu Y.-J., Brown R.A., Lau M.R., Shipley J.M., Fry M.J.;
RT "cDNA cloning of a third human C2-domain-containing class II
RT phosphoinositide 3-kinase, PI3K-C2gamma, and chromosomal assignment of this
RT gene (PIK3C2G) to 12p12.";
RL Genomics 54:569-574(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS LEU-146 AND
RP LEU-911.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-146 AND LEU-911.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [6]
RP VARIANT LEU-146.
RX PubMed=17991425; DOI=10.1016/j.bbrc.2007.10.180;
RA Daimon M., Sato H., Oizumi T., Toriyama S., Saito T., Karasawa S.,
RA Jimbu Y., Wada K., Kameda W., Susa S., Yamaguchi H., Emi M., Muramatsu M.,
RA Kubota I., Kawata S., Kato T.;
RT "Association of the PIK3C2G gene polymorphisms with type 2 DM in a Japanese
RT population.";
RL Biochem. Biophys. Res. Commun. 365:466-471(2008).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 1204-1307.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the phox homology domain of human phosphoinositide-3-
RT kinase-C2-gamma.";
RL Submitted (NOV-2009) to the PDB data bank.
CC -!- FUNCTION: Generates phosphatidylinositol 3-phosphate (PtdIns3P) and
CC phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as
CC second messengers (By similarity). May play a role in SDF1A-stimulated
CC chemotaxis (By similarity). {ECO:0000250|UniProtKB:O70167,
CC ECO:0000250|UniProtKB:O70173}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154;
CC Evidence={ECO:0000250|UniProtKB:O70173};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374;
CC Evidence={ECO:0000250|UniProtKB:O70173};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216;
CC EC=2.7.1.137; Evidence={ECO:0000250|UniProtKB:O70173};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710;
CC Evidence={ECO:0000250|UniProtKB:O70173};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O70167};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:O70167}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, prostate and testis.
CC Lower levels in small intestine, kidney and pancreas.
CC {ECO:0000269|PubMed:9878262}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00879, ECO:0000255|PROSITE-ProRule:PRU00880}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA03853.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ000008; CAA03853.1; ALT_SEQ; mRNA.
DR EMBL; AC087236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471094; EAW96387.1; -; Genomic_DNA.
DR EMBL; BC130277; AAI30278.1; -; mRNA.
DR CCDS; CCDS44839.1; -.
DR PIR; PC4347; PC4347.
DR RefSeq; NP_001275701.1; NM_001288772.1.
DR RefSeq; NP_001275703.1; NM_001288774.1.
DR RefSeq; NP_004561.3; NM_004570.5.
DR PDB; 2WWE; X-ray; 1.25 A; A=1204-1307.
DR PDBsum; 2WWE; -.
DR AlphaFoldDB; O75747; -.
DR SMR; O75747; -.
DR BioGRID; 111306; 2.
DR STRING; 9606.ENSP00000445381; -.
DR BindingDB; O75747; -.
DR ChEMBL; CHEMBL1163120; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; O75747; -.
DR GuidetoPHARMACOLOGY; 2288; -.
DR iPTMnet; O75747; -.
DR PhosphoSitePlus; O75747; -.
DR BioMuta; PIK3C2G; -.
DR MassIVE; O75747; -.
DR PaxDb; O75747; -.
DR PeptideAtlas; O75747; -.
DR PRIDE; O75747; -.
DR ProteomicsDB; 50178; -.
DR Antibodypedia; 23850; 118 antibodies from 28 providers.
DR DNASU; 5288; -.
DR Ensembl; ENST00000433979.6; ENSP00000404845.1; ENSG00000139144.11.
DR GeneID; 5288; -.
DR KEGG; hsa:5288; -.
DR UCSC; uc001rdt.4; human.
DR CTD; 5288; -.
DR DisGeNET; 5288; -.
DR GeneCards; PIK3C2G; -.
DR HGNC; HGNC:8973; PIK3C2G.
DR HPA; ENSG00000139144; Tissue enhanced (epididymis, stomach).
DR MalaCards; PIK3C2G; -.
DR MIM; 609001; gene.
DR neXtProt; NX_O75747; -.
DR OpenTargets; ENSG00000139144; -.
DR PharmGKB; PA33306; -.
DR VEuPathDB; HostDB:ENSG00000139144; -.
DR eggNOG; KOG0905; Eukaryota.
DR GeneTree; ENSGT00940000159982; -.
DR InParanoid; O75747; -.
DR OrthoDB; 204282at2759; -.
DR PhylomeDB; O75747; -.
DR TreeFam; TF102031; -.
DR BioCyc; MetaCyc:HS06583-MON; -.
DR BRENDA; 2.7.1.137; 2681.
DR BRENDA; 2.7.1.154; 2681.
DR PathwayCommons; O75747; -.
DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-HSA-1660514; Synthesis of PIPs at the Golgi membrane.
DR BioGRID-ORCS; 5288; 10 hits in 1071 CRISPR screens.
DR ChiTaRS; PIK3C2G; human.
DR EvolutionaryTrace; O75747; -.
DR GeneWiki; PIK3C2G; -.
DR GenomeRNAi; 5288; -.
DR Pharos; O75747; Tchem.
DR PRO; PR:O75747; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O75747; protein.
DR Bgee; ENSG00000139144; Expressed in corpus epididymis and 112 other tissues.
DR ExpressionAtlas; O75747; baseline and differential.
DR Genevisible; O75747; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; ISS:UniProtKB.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR GO; GO:0016307; F:phosphatidylinositol phosphate kinase activity; NAS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0044788; P:modulation by host of viral process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05177; PI3Kc_C2_gamma; 1.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.40.70; -; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR037707; PI3K-C2-gamma_dom.
DR InterPro; IPR002420; PI3K-type_C2_dom.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR000341; PI3K_Ras-bd_dom.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048; PTHR10048; 2.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chemotaxis; Kinase; Lipid metabolism; Membrane;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..1445
FT /note="Phosphatidylinositol 3-kinase C2 domain-containing
FT subunit gamma"
FT /id="PRO_0000088799"
FT DOMAIN 285..371
FT /note="PI3K-RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00879"
FT DOMAIN 453..628
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00880"
FT DOMAIN 643..819
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 888..1166
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 1199..1311
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 1328..1445
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 894..900
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1030..1038
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1049..1075
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT VARIANT 146
FT /note="P -> L (in dbSNP:rs11044004)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17991425, ECO:0000269|Ref.3"
FT /id="VAR_056676"
FT VARIANT 261
FT /note="A -> E (in dbSNP:rs7133666)"
FT /id="VAR_056677"
FT VARIANT 911
FT /note="P -> L (in dbSNP:rs12312266)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9878262, ECO:0000269|Ref.3"
FT /id="VAR_060323"
FT VARIANT 1290
FT /note="V -> G (in dbSNP:rs12099555)"
FT /id="VAR_060324"
FT VARIANT 1442
FT /note="N -> T (in dbSNP:rs12816860)"
FT /id="VAR_060325"
FT CONFLICT 129
FT /note="Missing (in Ref. 3; EAW96387 and 4; AAI30278)"
FT /evidence="ECO:0000305"
FT CONFLICT 965
FT /note="G -> R (in Ref. 1; CAA03853)"
FT /evidence="ECO:0000305"
FT CONFLICT 1209
FT /note="Missing (in Ref. 1; CAA03853)"
FT /evidence="ECO:0000305"
FT CONFLICT 1314
FT /note="Missing (in Ref. 1; CAA03853)"
FT /evidence="ECO:0000305"
FT CONFLICT 1323
FT /note="E -> EK (in Ref. 1; CAA03853)"
FT /evidence="ECO:0000305"
FT CONFLICT 1377
FT /note="R -> L (in Ref. 1; CAA03853)"
FT /evidence="ECO:0000305"
FT STRAND 1202..1214
FT /evidence="ECO:0007829|PDB:2WWE"
FT STRAND 1217..1227
FT /evidence="ECO:0007829|PDB:2WWE"
FT STRAND 1232..1237
FT /evidence="ECO:0007829|PDB:2WWE"
FT HELIX 1239..1252
FT /evidence="ECO:0007829|PDB:2WWE"
FT TURN 1253..1255
FT /evidence="ECO:0007829|PDB:2WWE"
FT HELIX 1267..1271
FT /evidence="ECO:0007829|PDB:2WWE"
FT HELIX 1273..1287
FT /evidence="ECO:0007829|PDB:2WWE"
FT HELIX 1292..1295
FT /evidence="ECO:0007829|PDB:2WWE"
FT HELIX 1298..1305
FT /evidence="ECO:0007829|PDB:2WWE"
SQ SEQUENCE 1445 AA; 165715 MW; 8D02A3620AE4318D CRC64;
MAYSWQTDPN PNESHEKQYE HQEFLFVNQP HSSSQVSLGF DQIVDEISGK IPHYESEIDE
NTFFVPTAPK WDSTGHSLNE AHQISLNEFT SKSRELSWHQ VSKAPAIGFS PSVLPKPQNT
NKECSWGSPI GKHHGADDSR FSILAPSFTS LDKINLEKEL ENENHNYHIG FESSIPPTNS
SFSSDFMPKE ENKRSGHVNI VEPSLMLLKG SLQPGMWEST WQKNIESIGC SIQLVEVPQS
SNTSLASFCN KVKKIRERYH AADVNFNSGK IWSTTTAFPY QLFSKTKFNI HIFIDNSTQP
LHFMPCANYL VKDLIAEILH FCTNDQLLPK DHILSVCGSE EFLQNDHCLG SHKMFQKDKS
VIQLHLQKSR EAPGKLSRKH EEDHSQFYLN QLLEFMHIWK VSRQCLLTLI RKYDFHLKYL
LKTQENVYNI IEEVKKICSV LGCVETKQIT DAVNELSLIL QRKGENFYQS SETSAKGLIE
KVTTELSTSI YQLINVYCNS FYADFQPVNV PRCTSYLNPG LPSHLSFTVY AAHNIPETWV
HRINFPLEIK SLPRESMLTV KLFGIACATN NANLLAWTCL PLFPKEKSIL GSMLFSMTLQ
SEPPVEMITP GVWDVSQPSP VTLQIDFPAT GWEYMKPDSE ENRSNLEEPL KECIKHIARL
SQKQTPLLLS EEKKRYLWFY RFYCNNENCS LPLVLGSAPG WDERTVSEMH TILRRWTFSQ
PLEALGLLTS SFPDQEIRKV AVQQLDNLLN DELLEYLPQL VQAVKFEWNL ESPLVQLLLH
RSLQSIQVAH RLYWLLKNAE NEAYFKSWYQ KLLAALQFCA GKALNDEFSK EQKLIKILGD
IGERVKSASD HQRQEVLKKE IGRLEEFFQD VNTCHLPLNP ALCIKGIDHD ACSYFTSNAL
PLKITFINAN PMGKNISIIF KAGDDLRQDM LVLQLIQVMD NIWLQEGLDM QMIIYRCLST
GKDQGLVQMV PDAVTLAKIH RHSGLIGPLK ENTIKKWFSQ HNHLKADYEK ALRNFFYSCA
GWCVVTFILG VCDRHNDNIM LTKSGHMFHI DFGKFLGHAQ TFGGIKRDRA PFIFTSEMEY
FITEGGKNPQ HFQDFVELCC RAYNIIRKHS QLLLNLLEMM LYAGLPELSG IQDLKYVYNN
LRPQDTDLEA TSHFTKKIKE SLECFPVKLN NLIHTLAQMS AISPAKSTSQ TFPQESCLLS
TTRSIERATI LGFSKKSSNL YLIQVTHSNN ETSLTEKSFE QFSKLHSQLQ KQFASLTLPE
FPHWWHLPFT NSDHRRFRDL NHYMEQILNV SHEVTNSDCV LSFFLSEAVQ QTVEESSPVY
LGEKFPDKKP KVQLVISYED VKLTILVKHM KNIHLPDGSA PSAHVEFYLL PYPSEVRRRK
TKSVPKCTDP TYNEIVVYDE VTELQGHVLM LIVKSKTVFV GAINIRLCSV PLDKEKWYPL
GNSII
